Values CatLog read from this paper

Use of endoproteases to identify catalytic domains, linker regions, and functional interactions in soluble peptidylglycine alpha-amidating monooxygenase

PMID 8486658doi:10.1016/s0021-9258(18)98406-1Open in Browse

The paper itself is not on this site: read it at the publisher. This page lists only the values CatLog read from it.

CatLog read 9 records (16 values) from this paper: peptidylglycine alpha-hydroxylating monooxygenase (PHM) activity of PAM, peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity of PAM from Rattus norvegicus.

Read from the paper by an AI model and checked against the paper by a second, separate AI run; code converted the units. Values are in CatLog's units; each record opens in Browse with the line the paper prints and the checks. CatLog calculated the 7 kcat/Km values marked “calc.” from kcat and Km; no printed kcat/Km was read for those records.

EC 1.14.17.3, EC 4.3.2.5

Records read from this paper
EnzymeOrganismSubstratekcat (s⁻¹)Km (mM)kcat/Km (mM⁻¹ s⁻¹)ConditionsOpen record
peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity of PAMRattus norvegicusN-acetyl-L-tyrosyl-L-valyl-alpha-hydroxyglycinesecreted by stably transfected hEK-293 cells; purified920.0372.5 × 10³ calc.pH 5.5, 37 °COpen record: peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity of PAM, N-acetyl-L-tyrosyl-L-valyl-alpha-hydroxyglycine
peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity of PAMRattus norvegicusN-acetyl-L-tyrosyl-L-valyl-alpha-hydroxyglycine860.0342.5 × 10³ calc.pH 5.5, 37 °COpen record: peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity of PAM, N-acetyl-L-tyrosyl-L-valyl-alpha-hydroxyglycine
peptidylglycine alpha-hydroxylating monooxygenase (PHM) activity of PAMRattus norvegicusN-acetyl-L-tyrosyl-L-valyl-glycinesecreted by stably transfected hEK-293 cells; purified70.014500 calc.pH 5.5, 37 °COpen record: peptidylglycine alpha-hydroxylating monooxygenase (PHM) activity of PAM, N-acetyl-L-tyrosyl-L-valyl-glycine
peptidylglycine alpha-hydroxylating monooxygenase (PHM) activity of PAMRattus norvegicusN-acetyl-L-tyrosyl-L-valyl-glycineTable II160.0082.0 × 10³ calc.pH 5.5, 37 °COpen record: peptidylglycine alpha-hydroxylating monooxygenase (PHM) activity of PAM, N-acetyl-L-tyrosyl-L-valyl-glycine
peptidylglycine alpha-hydroxylating monooxygenase (PHM) activity of PAMRattus norvegicusN-acetyl-L-tyrosyl-L-valyl-glycineTable II140.0091.6 × 10³ calc.pH 5.5, 37 °COpen record: peptidylglycine alpha-hydroxylating monooxygenase (PHM) activity of PAM, N-acetyl-L-tyrosyl-L-valyl-glycine
peptidylglycine alpha-hydroxylating monooxygenase (PHM) activity of PAMRattus norvegicusN-acetyl-L-tyrosyl-L-valyl-glycinerPAM-3 digested with endoprotease Lys-C (36-kDa PHM protein)170.0111.5 × 10³ calc.pH 5.5, 37 °COpen record: peptidylglycine alpha-hydroxylating monooxygenase (PHM) activity of PAM, N-acetyl-L-tyrosyl-L-valyl-glycine
peptidylglycine alpha-hydroxylating monooxygenase (PHM) activity of PAMRattus norvegicusN-acetyl-L-tyrosyl-L-valyl-glycinerPHM-s pool C; secreted by hEK-293 cells; Table II40.018220 calc.pH 5.5, 37 °COpen record: peptidylglycine alpha-hydroxylating monooxygenase (PHM) activity of PAM, N-acetyl-L-tyrosyl-L-valyl-glycine
peptidylglycine alpha-hydroxylating monooxygenase (PHM) activity of PAMRattus norvegicusN-acetyl-L-tyrosyl-L-valyl-glycinesecreted by stably transfected hEK-293 cells; purified—0.018—pH 5.5, 37 °COpen record: peptidylglycine alpha-hydroxylating monooxygenase (PHM) activity of PAM, N-acetyl-L-tyrosyl-L-valyl-glycine
peptidylglycine alpha-hydroxylating monooxygenase (PHM) activity of PAMRattus norvegicusN-acetyl-L-tyrosyl-L-valyl-glycinerPAM-3 digested with trypsin (0.1 µg trypsin/ug PAM-3)—0.008—pH 5.5, 37 °COpen record: peptidylglycine alpha-hydroxylating monooxygenase (PHM) activity of PAM, N-acetyl-L-tyrosyl-L-valyl-glycine